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Updated: Jan 7, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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Published on: September 28, 2022

Site-Selective Protein Modification via Peptide-Directed Proximity Catalysis.

Laetitia Raynal^1,2, Joe Nabarro^1,2, Lisa M Miller^2,3

¹Department of Chemistry, University of York, Heslington YO10 5DD, U.K.

|January 5, 2026

Summary

This summary is machine-generated.

Catalyst-functionalized peptides enable precise protein modification through proximity catalysis. Researchers can tune modification sites by altering peptide-catalyst structure for diverse applications.

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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

Biochemistry
Chemical Biology
Protein Engineering

Background:

Proximity catalysis enables localized protein modification via ligand binding.
Developing versatile ligands is key for advancing this technique.

Purpose of the Study:

Introduce catalyst-functionalized peptides as adaptable ligands for proximity catalysis.
Demonstrate site-selective protein modification using these novel peptide ligands.

Main Methods:

Functionalized target-binding peptides with pyridinium oxime catalysts.
Utilized N-acyl-N-alkylsulfonamide reagents for protein modification.
Investigated the impact of catalyst position on modification site.

Main Results:

Achieved site-selective modification of model proteins.
Successfully introduced functionalities like fluorophores and affinity handles.
Demonstrated that altering catalyst position on the peptide tunes the modification site.

Conclusions:

Catalyst-functionalized peptides are effective ligands for proximity catalysis.
Peptide-catalyst design offers control over protein modification sites.
This approach facilitates the development of tailored protein modification strategies.